1ID8
NMR STRUCTURE OF GLUTAMATE MUTASE (B12-BINDING SUBUNIT) COMPLEXED WITH THE VITAMIN B12 NUCLEOTIDE
Summary for 1ID8
Entry DOI | 10.2210/pdb1id8/pdb |
Related | 1CB7 1FMF |
Descriptor | METHYLASPARTATE MUTASE S CHAIN, 2-HYDROXY-PROPYL-AMMONIUM, PHOSPHORIC ACID MONO-[5-(5,6-DIMETHYL-BENZOIMIDAZOL-1-YL)-4-HYDROXY-2-HYDROXYMETHYL-TETRAHYDRO-FURAN-3-YL] ESTER (3 entities in total) |
Functional Keywords | coenzyme b12, ligand binding, nucleotide, protein nmr spectroscopy, protein folding, isomerase |
Biological source | Clostridium tetanomorphum |
Total number of polymer chains | 1 |
Total formula weight | 15198.26 |
Authors | Tollinger, M.,Eichmuller, C.,Konrat, R.,Huhta, M.S.,Marsh, E.N.G.,Krautler, B. (deposition date: 2001-04-04, release date: 2001-06-27, Last modification date: 2024-05-22) |
Primary citation | Tollinger, M.,Eichmuller, C.,Konrat, R.,Huhta, M.S.,Marsh, E.N.,Krautler, B. The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12). J.Mol.Biol., 309:777-791, 2001 Cited by PubMed: 11397096DOI: 10.1006/jmbi.2001.4696 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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